TBL17_ARATH
ID TBL17_ARATH Reviewed; 501 AA.
AC Q9FHM0;
DT 11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Protein YLS7;
DE AltName: Full=Protein TRICHOME BIREFRINGENCE-LIKE 17;
DE AltName: Full=Protein YELLOW-LEAF-SPECIFIC GENE 7;
GN Name=YLS7; Synonyms=TBL17; OrderedLocusNames=At5g51640; ORFNames=K17N15.19;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP INDUCTION.
RX PubMed=11230571; DOI=10.1093/pcp/pce021;
RA Yoshida S., Ito M., Nishida I., Watanabe A.;
RT "Isolation and RNA gel blot analysis of genes that could serve as potential
RT molecular markers for leaf senescence in Arabidopsis thaliana.";
RL Plant Cell Physiol. 42:170-178(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP GENE FAMILY.
RC STRAIN=cv. Columbia;
RX PubMed=17316173; DOI=10.1111/j.1365-313x.2006.02994.x;
RA Xin Z., Mandaokar A., Chen J., Last R.L., Browse J.;
RT "Arabidopsis ESK1 encodes a novel regulator of freezing tolerance.";
RL Plant J. 49:786-799(2007).
RN [6]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=20388664; DOI=10.1104/pp.110.153320;
RA Bischoff V., Nita S., Neumetzler L., Schindelasch D., Urbain A., Eshed R.,
RA Persson S., Delmer D., Scheible W.R.;
RT "TRICHOME BIREFRINGENCE and its homolog AT5G01360 encode plant-specific
RT DUF231 proteins required for cellulose biosynthesis in Arabidopsis.";
RL Plant Physiol. 153:590-602(2010).
RN [7]
RP 3D-STRUCTURE MODELING.
RX PubMed=20657172; DOI=10.4161/psb.5.8.12414;
RA Bischoff V., Selbig J., Scheible W.R.;
RT "Involvement of TBL/DUF231 proteins into cell wall biology.";
RL Plant Signal. Behav. 5:1057-1059(2010).
CC -!- FUNCTION: May act as a bridging protein that binds pectin and other
CC cell wall polysaccharides. Probably involved in maintaining
CC esterification of pectins (By similarity). May be involved in the
CC specific O-acetylation of cell wall polymers (By similarity).
CC {ECO:0000250|UniProtKB:Q9FG35, ECO:0000250|UniProtKB:Q9LY46}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
CC membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, cauline leaves and flowers.
CC {ECO:0000269|PubMed:11230571}.
CC -!- DEVELOPMENTAL STAGE: Up-regulated in leaves during natural senescence.
CC {ECO:0000269|PubMed:11230571}.
CC -!- INDUCTION: By dark. {ECO:0000269|PubMed:11230571}.
CC -!- MISCELLANEOUS: Contains 2 motifs that are conserved in esterases, but
CC it is unlikely that this protein belongs to the catalytically active
CC pectin esterases. {ECO:0000305|PubMed:20657172}.
CC -!- SIMILARITY: Belongs to the PC-esterase family. TBL subfamily.
CC {ECO:0000305}.
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DR EMBL; AB047810; BAB32887.1; -; mRNA.
DR EMBL; AB018109; BAB08680.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96110.1; -; Genomic_DNA.
DR EMBL; AY080801; AAL87282.1; -; mRNA.
DR EMBL; AY133873; AAM91807.1; -; mRNA.
DR RefSeq; NP_199977.1; NM_124543.3.
DR AlphaFoldDB; Q9FHM0; -.
DR SMR; Q9FHM0; -.
DR PaxDb; Q9FHM0; -.
DR PRIDE; Q9FHM0; -.
DR ProteomicsDB; 232988; -.
DR EnsemblPlants; AT5G51640.1; AT5G51640.1; AT5G51640.
DR GeneID; 835238; -.
DR Gramene; AT5G51640.1; AT5G51640.1; AT5G51640.
DR KEGG; ath:AT5G51640; -.
DR Araport; AT5G51640; -.
DR TAIR; locus:2153077; AT5G51640.
DR eggNOG; ENOG502QTC6; Eukaryota.
DR HOGENOM; CLU_020953_6_3_1; -.
DR InParanoid; Q9FHM0; -.
DR OMA; KSYENWR; -.
DR OrthoDB; 739025at2759; -.
DR PhylomeDB; Q9FHM0; -.
DR PRO; PR:Q9FHM0; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FHM0; baseline and differential.
DR Genevisible; Q9FHM0; AT.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0000138; C:Golgi trans cisterna; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016413; F:O-acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0010150; P:leaf senescence; IEP:TAIR.
DR InterPro; IPR026057; PC-Esterase.
DR InterPro; IPR029962; TBL.
DR InterPro; IPR029983; TBL17(YLS7)/TBL18.
DR InterPro; IPR025846; TBL_N.
DR PANTHER; PTHR32285; PTHR32285; 1.
DR PANTHER; PTHR32285:SF158; PTHR32285:SF158; 1.
DR Pfam; PF13839; PC-Esterase; 1.
DR Pfam; PF14416; PMR5N; 1.
PE 2: Evidence at transcript level;
KW Membrane; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..501
FT /note="Protein YLS7"
FT /id="PRO_0000424704"
FT TRANSMEM 25..45
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT REGION 69..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 438..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 211..213
FT /note="GDS motif"
FT MOTIF 467..481
FT /note="DCXHWCLPGXXDXWN motif"
FT COMPBIAS 76..91
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..112
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 443..457
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 501 AA; 56526 MW; 7AB4739CBF50FD98 CRC64;
MTLASPRVSN SKTTVLLFPR KVSSIAFAIG GLTSFVIFAS LLLFTYPIGS SVTDYFYRTE
TTQNVQFHHS IHDPDRNPSP VSSSESPPVL TQDSDDKVLP KGSHDSNDVR LGEETNSGKS
SNVSIDEEAT QDHVETECDL YHGNWFYDPM GPLYTNNSCP LLTQMQNCQG NGRPDKGYEN
WRWKPSQCDL PRFDAKKFLE LMRGKTLAFI GDSVARNQME SMMCLLWQVE TPVNRGNRKM
QRWYFRSSSV MIARMWSSWL VHQFNEPFGF ATDGVTKLKL DQPDERIIEA LPNFDVVVLS
SGHWFAKQSV YILNDQIVGG QLWWPDKSKP EKINNVEAFG ISVETIIKAM AKHPNYTGLT
ILRTWSPDHY EGGAWNTGGS CTGKVEPLPP GNLVTNGFTE IMHEKQATGF HRAVADDKLG
NRSKKLKLMD ITEAFGYRHD GHPGPYRSPD PKKITKRGPD GQPPPQDCLH WCMPGPVDTW
NEMVLEIIRR DFEGRQSSPS S
